Three Antigenic Regions in p17 of Human Immunodeficiency Virus Type 1 (HIV-1) Revealed by Mouse Monoclonal Antibodies and Human Antibodies in HIV-1 Carrier Sera

• Published in: MICROBIOLOGY and IMMUNOLOGY 1995, Vol.39(10), pp.775-785
• Main Authors: Liu, Xiaoliang, Ota, Akemi, Watanabe, Michiko, Ueda, Shigeharu, Saitoh, Atsushi, Shinagawa, Hideo, Nakata, Atsuo, Kurimura, Takashi, Wang, Xiaoui, Zhao, Yu, Kondo, Kiyoshi, Seki, Jiro, Miyake, Shinichi, Sakato, Nobuo, Fujio, Hajime
• Format: Article
• Language: English
• Subjects: AIDS/HIV; Amino Acid Sequence; Animals; Antibodies, Monoclonal - blood; Antibodies, Monoclonal - chemistry; Antigenic regions; Binding Sites, Antibody; Biological and medical sciences; Carrier State - immunology; Carrier State - virology; Enzyme-Linked Immunosorbent Assay; Epitope Mapping; Fluorescent Antibody Technique, Indirect; Fundamental and applied biological sciences. Psychology; gag Gene Products, Human Immunodeficiency Virus; Gene Products, gag - chemistry; Gene Products, gag - immunology; HIV Antibodies - blood; HIV Antigens - chemistry; HIV Antigens - immunology; HIV Infections - blood; HIV Infections - immunology; HIV-1 - immunology; Human antibodies; Human immunodeficiency virus 1; Humans; Mice; Microbiology; Molecular Sequence Data; Monoclonal antibodies; Morphology, structure, chemical composition, physicochemical properties; p17 of HIV-1; Viral Proteins; Virology
• ISSN: 0385-5600; 1348-0421
• DOI: 10.1111/j.1348-0421.1995.tb03270.x

We investigated the murine antibody response to recombinant p17 (rp17) of human immunodeficiency virus type 1 (HIV-1) and the human antibody response directed to p17 in HIV-1 infection. Three large peptides covering residues 12-29, 53-87 and 87-115 of p17 were synthesized. The cysteine residues 57 and 87 of peptide 53-87 were reoxidized to form a disulfide bridge. Eighteen out of 19 murine monoclonal anti-rp17 antibodies had relatively high affinities (KA=1.9×105-1.4×108M-1) with one of the 3 p17 peptides in the liquid phase. Each monoclonal antibody reacted only with one particular peptide and had no reactivity with the other 2 p17 peptides. All the monoclonal antibodies reacted with rp17 in the liquid phase with a reasonable degree of affinity (KA=2.0×105-1.8×107M-1). Four HIV-1 carrier sera, which were positive in ELISA using rp17 as the antigen, reacted positively in an ELISA using 3 p17 peptides which were used to titrate murine monoclonal antibodies. Murine monoclonal antibodies having specificity for the 3 p17 peptides stained live HIV-1-infected cells by means of indirect membrane immunofluorescence, irrespective of their specificity. This suggests that the various portions of p17 (at least 3 regions of p17) were exposed on the surface of live infected cells, probably as short polypeptide chains.